Structure of PDB 3arq Chain A

Receptor sequence
>3arqA (length=575) Species: 669 (Vibrio harveyi) [Search protein sequence]
APTAPSIDMYGSNNLQFSKIELAMETTSGYNDMVKYHELAKIKVKFNQWS
GTSGDTYNVYFDGVKVATGAITGSQTTASFEYGQGGLYQMEIEACDATGC
SKSAPVEITIADTDGSHLKPLTMNVDPNNKSYNTDPSIVMGTYFVEWGIY
GRDYTVDNMPVDNLTHILYGFIPICGPNESVKSVGGNSFNALQTACRGVN
DYEVVIHDPWAAYQKSFPQAGHEYSTPIKGNYAMLMALKQRNPDLKIIPS
IGGWTLSDPFYDFVDKKNRDTFVASVKKFLKTWKFYDGVDIDWEFPGGGG
AAADKGDPVNDGPAYIALMRELRVMLDELEAETGRTYELTSAIGVGYDKI
EDVDYADAVQYMDYIFAMTYDFYGGWNNVPGHQTALYCGSFMRPGQCDGG
GVDENGEPYKGPAYTADNGIQLLLAQGVPANKLVLGTAMYGRGWEGVTPD
TLTDPNDPMTGTATGKLKGSTAQGVWEDGVIDYKGIKSFMLGANNTGING
FEYGYDAQAEAPWVWNRSTGELITFDDHRSVLAKGNYAKSLGLAGLFSWE
IDADNGDILNAMHEGMAGGVVTPPN
3D structure
PDB3arq Potent family-18 chitinase inhibitors: x-ray structures, affinities, and binding mechanisms
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D311 D313 E315 Y391
Catalytic site (residue number reindexed from 1) D290 D292 E294 Y370
Enzyme Commision number 3.2.1.14: chitinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 DM5 A W275 G320 D392 W397 Y435 W254 G299 D371 W376 Y414 PDBbind-CN: -logKd/Ki=6.40,Kd=0.4uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004568 chitinase activity
GO:0008061 chitin binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006032 chitin catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3arq, PDBe:3arq, PDBj:3arq
PDBsum3arq
PubMed21531720
UniProtQ9AMP1

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